메뉴 건너뛰기




Volumn 55, Issue 6, 1998, Pages 577-594

Mechanisms of trafficking in axons and dendrites: Implications for development and neurodegeneration

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID PRECURSOR PROTEIN;

EID: 0032144774     PISSN: 03010082     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0301-0082(98)00021-5     Document Type: Article
Times cited : (48)

References (138)
  • 1
    • 0029093287 scopus 로고
    • Microtubules released from the neuronal centrosome are transported into the axon
    • Ahmad F. J., Baas P. W. Microtubules released from the neuronal centrosome are transported into the axon. J. Cell Sci. 108:1995;2761-2769.
    • (1995) J. Cell Sci. , vol.108 , pp. 2761-2769
    • Ahmad, F.J.1    Baas, P.W.2
  • 2
    • 0027367040 scopus 로고
    • Transport and localization of exogenous myelin basic protein mRNA microinjected into oligodendrocytes
    • Ainger K., Avossa D., Morgan F., Hill S. J., Barry C., Barbarese E., Carson J. H. Transport and localization of exogenous myelin basic protein mRNA microinjected into oligodendrocytes. J. Cell Biol. 123:1993;431-441.
    • (1993) J. Cell Biol. , vol.123 , pp. 431-441
    • Ainger, K.1    Avossa, D.2    Morgan, F.3    Hill, S.J.4    Barry, C.5    Barbarese, E.6    Carson, J.H.7
  • 3
    • 0025035790 scopus 로고
    • Molecular cloning of a ubiquitously distributed microtubule-associated protein with Mr 190 000
    • Aizawa H., Emori Y., Mirofushi H., Kawasaki H., Sakai H., Suzuki K. Molecular cloning of a ubiquitously distributed microtubule-associated protein with Mr 190 000. J. biol. Chem. 265:1990;13849-13855.
    • (1990) J. Biol. Chem. , vol.265 , pp. 13849-13855
    • Aizawa, H.1    Emori, Y.2    Mirofushi, H.3    Kawasaki, H.4    Sakai, H.5    Suzuki, K.6
  • 5
    • 0031048886 scopus 로고    scopus 로고
    • Microtubules and axonal growth
    • Baas P. W. Microtubules and axonal growth. Curr. Opin. Cell Biol. 9:1997;29-36.
    • (1997) Curr. Opin. Cell Biol. , vol.9 , pp. 29-36
    • Baas, P.W.1
  • 6
    • 0030344902 scopus 로고    scopus 로고
    • The neuronal centrosome as a generator of microtubules for the axon
    • Baas P. W. The neuronal centrosome as a generator of microtubules for the axon. Curr. Top. Dev. Biol. 33:1997;281-298.
    • (1997) Curr. Top. Dev. Biol. , vol.33 , pp. 281-298
    • Baas, P.W.1
  • 7
    • 0030114484 scopus 로고    scopus 로고
    • A composite model for establishing the microtubule arrays of the neuron
    • Baas P. W., Yu W. A composite model for establishing the microtubule arrays of the neuron. Molec. Neurol. 12:1996;145-161.
    • (1996) Molec. Neurol. , vol.12 , pp. 145-161
    • Baas, P.W.1    Yu, W.2
  • 8
    • 0342419162 scopus 로고
    • Polarity orientation of microtubules in hippocampal neurons: Uniformity in the axon and nonuniformity in the dendrite
    • Baas P. W., Deitch J. S., Black M. M., Banker G. A. Polarity orientation of microtubules in hippocampal neurons: uniformity in the axon and nonuniformity in the dendrite. Proc. natl. Acad. Sci. U.S.A. 85:1988;8335-8339.
    • (1988) Proc. Natl. Acad. Sci. U.S.A. , vol.85 , pp. 8335-8339
    • Baas, P.W.1    Deitch, J.S.2    Black, M.M.3    Banker, G.A.4
  • 9
    • 0029962216 scopus 로고    scopus 로고
    • Going mobile: Microtubule motors and chromosome segregation
    • Barton N. R., Goldstein L. S. B. Going mobile: microtubule motors and chromosome segregation. Proc. natl. Acad. Sci. U.S.A. 93:1996;1735-1742.
    • (1996) Proc. Natl. Acad. Sci. U.S.A. , vol.93 , pp. 1735-1742
    • Barton, N.R.1    Goldstein, L.S.B.2
  • 10
    • 0028051579 scopus 로고
    • Microtubule transport and assembly cooperate to generate the microtubule array of growing axons
    • Black M. M. Microtubule transport and assembly cooperate to generate the microtubule array of growing axons. Prog. Brain. Res. 102:1994;61-77.
    • (1994) Prog. Brain. Res. , vol.102 , pp. 61-77
    • Black, M.M.1
  • 12
    • 0029449733 scopus 로고
    • Motor proteins 1: Kinesins
    • Bloom G. S., Endow S. A. Motor proteins 1: kinesins. Protein Profiles. 2:1995;1109-1111.
    • (1995) Protein Profiles , vol.2 , pp. 1109-1111
    • Bloom, G.S.1    Endow, S.A.2
  • 13
    • 0023944514 scopus 로고
    • Native structure and physical properties of bovine brain kinesin and identification of the ATP-binding subunit polypeptide
    • Bloom G. S., Wagner M. C., Pfister K. K., Brady S. T. Native structure and physical properties of bovine brain kinesin and identification of the ATP-binding subunit polypeptide. Biochemistry. 27:1988;3409-3416.
    • (1988) Biochemistry , vol.27 , pp. 3409-3416
    • Bloom, G.S.1    Wagner, M.C.2    Pfister, K.K.3    Brady, S.T.4
  • 14
    • 0026049509 scopus 로고
    • Molecular motors in the nervous system
    • Brady S. T. Molecular motors in the nervous system. Neuron. 7:1991;521-533.
    • (1991) Neuron , vol.7 , pp. 521-533
    • Brady, S.T.1
  • 15
    • 0028829598 scopus 로고
    • Biochemical and functional diversity of microtubule motors in the nervous system
    • Brady S. T., Sperry A. O. Biochemical and functional diversity of microtubule motors in the nervous system. Curr. Opin. Neurobiol. 5:1995;551-558.
    • (1995) Curr. Opin. Neurobiol. , vol.5 , pp. 551-558
    • Brady, S.T.1    Sperry, A.O.2
  • 16
    • 0020419627 scopus 로고
    • Fast axonal transport in extruded axoplasm from squid giant axon
    • Brady S. T., Lasek R. J., Allen R. D. Fast axonal transport in extruded axoplasm from squid giant axon. Science. 218:1982;1129-1131.
    • (1982) Science , vol.218 , pp. 1129-1131
    • Brady, S.T.1    Lasek, R.J.2    Allen, R.D.3
  • 17
    • 0027308924 scopus 로고
    • Abnormal tau phosphorylation at Ser396 in Alzheimer's disease recapitulates development and contributes to reduced microtubule binding
    • Bramblett G. T., Goedert M., Jakes R., Merrick S. E., Trojanowski J. Q., Lee V. M.-Y. Abnormal tau phosphorylation at Ser396 in Alzheimer's disease recapitulates development and contributes to reduced microtubule binding. Neuron. 10:1993;1089-1099.
    • (1993) Neuron , vol.10 , pp. 1089-1099
    • Bramblett, G.T.1    Goedert, M.2    Jakes, R.3    Merrick, S.E.4    Trojanowski, J.Q.5    Lee, V.M.-Y.6
  • 18
    • 0025988453 scopus 로고
    • Transport complexes associated with slow axonal flow
    • Bray J. J., Mills R. G. Transport complexes associated with slow axonal flow. Neurochem. Res. 16:1991;645-649.
    • (1991) Neurochem. Res. , vol.16 , pp. 645-649
    • Bray, J.J.1    Mills, R.G.2
  • 19
    • 0013576148 scopus 로고
    • Self-assembly of HeLa tubulin and the identification of HeLa microtubule-associated proteins
    • Bulinski J. C., Borisy G. G. Self-assembly of HeLa tubulin and the identification of HeLa microtubule-associated proteins. Proc. natl. Acad. Sci. U.S.A. 76:1979;293-297.
    • (1979) Proc. Natl. Acad. Sci. U.S.A. , vol.76 , pp. 293-297
    • Bulinski, J.C.1    Borisy, G.G.2
  • 20
    • 0019292829 scopus 로고
    • Widespread distribution of a 210 000 mol wt microtubule-associated protein in cells and tissues of primates
    • Bulinski J. C., Borisy G. G. Widespread distribution of a 210 000 mol wt microtubule-associated protein in cells and tissues of primates. J. Cell Biol. 87:1980;802-808.
    • (1980) J. Cell Biol. , vol.87 , pp. 802-808
    • Bulinski, J.C.1    Borisy, G.G.2
  • 22
    • 0025098891 scopus 로고
    • Inhibition of neurite polarity by antisense oligonucleotides in primary cerebellar neurons
    • Caceres A., Kosik K. S. Inhibition of neurite polarity by antisense oligonucleotides in primary cerebellar neurons. Nature. 343:1990;461-463.
    • (1990) Nature , vol.343 , pp. 461-463
    • Caceres, A.1    Kosik, K.S.2
  • 23
    • 0029849616 scopus 로고    scopus 로고
    • Delivery of newly synthesized tubulin to rapidly growing distal axons of sympathetic neurons in compartmental cultures
    • Campenot B., Lund K., Senger D. L. Delivery of newly synthesized tubulin to rapidly growing distal axons of sympathetic neurons in compartmental cultures. J. Cell Biol. 135:1996;701-709.
    • (1996) J. Cell Biol. , vol.135 , pp. 701-709
    • Campenot, B.1    Lund, K.2    Senger, D.L.3
  • 24
    • 0028351791 scopus 로고
    • Morphological and bioxhemical analysis of the intracellular trafficking of the Alzheimer's β/A4 amyloid precursor protein
    • Caporaso G. L., Takei K., Ggandy S. E., Matteoli M., Mundigl O., Greengard P., De Camilli P. Morphological and bioxhemical analysis of the intracellular trafficking of the Alzheimer's β/A4 amyloid precursor protein. J. Neurosci. 14:1994;3122-3138.
    • (1994) J. Neurosci. , vol.14 , pp. 3122-3138
    • Caporaso, G.L.1    Takei, K.2    Ggandy, S.E.3    Matteoli, M.4    Mundigl, O.5    Greengard, P.6    De Camilli, P.7
  • 25
    • 0025959396 scopus 로고
    • Non-neuronal 210 kD microtubule-associated protein (MAP4) contains a domain homologous to the microtubule-binding domains of MAP2 and tau
    • Chapin S., Bulinski J. C. Non-neuronal 210 kD microtubule-associated protein (MAP4) contains a domain homologous to the microtubule-binding domains of MAP2 and tau. J. Cell Sci. 98:1991;27-36.
    • (1991) J. Cell Sci. , vol.98 , pp. 27-36
    • Chapin, S.1    Bulinski, J.C.2
  • 26
    • 0027085694 scopus 로고
    • Microtubule stabilization by assembly promoting microtubule-associated proteins: A repeat performance
    • Chapin S., Bulinski J. C. Microtubule stabilization by assembly promoting microtubule-associated proteins: a repeat performance. Cell Motil. Cytoskeleton. 4:1992;236-243.
    • (1992) Cell Motil. Cytoskeleton , vol.4 , pp. 236-243
    • Chapin, S.1    Bulinski, J.C.2
  • 27
    • 0017758306 scopus 로고
    • Physical and chemical properties of purified tau factor and the role of tau in microtubule assembly
    • Cleveland D. W., Hwo S.-Y., Kirschner M. W. Physical and chemical properties of purified tau factor and the role of tau in microtubule assembly. J. Molec. Biol. 116:1977;227-247.
    • (1977) J. Molec. Biol. , vol.116 , pp. 227-247
    • Cleveland, D.W.1    Hwo, S.-Y.2    Kirschner, M.W.3
  • 28
    • 0029912056 scopus 로고    scopus 로고
    • Mechanisms of neuronal death in Alzheimer's disease
    • Cotman C. W., Su J. H. Mechanisms of neuronal death in Alzheimer's disease. Brain Pathol. 6:1996;493-506.
    • (1996) Brain Pathol. , vol.6 , pp. 493-506
    • Cotman, C.W.1    Su, J.H.2
  • 29
    • 0002826363 scopus 로고    scopus 로고
    • The β-amyloid Model of Alzheimer's disease
    • Eds. W. Wasco and R. E. Tanzi. Humana Press, Totowa, NJ
    • Cotman, C. W., Cribbs, D. H. and Anderson, A. J. (1996) The β-amyloid Model of Alzheimer's disease. In: Molecular Mechanisms of Dementia, pp. 73-90. Eds. W. Wasco and R. E. Tanzi. Humana Press, Totowa, NJ.
    • (1996) In: Molecular Mechanisms of Dementia , pp. 73-90
    • Cotman, C.W.1    Cribbs, D.H.2    Anderson, A.J.3
  • 31
    • 0000875128 scopus 로고
    • Aβ induces increased expression and processing of amyloid precursor protein in cortical neurons
    • Cribbs D. H., Davis-Salinas J., Cotman C. W., Van Nostrand W. E. Aβ induces increased expression and processing of amyloid precursor protein in cortical neurons. Alzheimer's Research. 1(4):1995;197-200.
    • (1995) Alzheimer's Research , vol.1 , Issue.4 , pp. 197-200
    • Cribbs, D.H.1    Davis-Salinas, J.2    Cotman, C.W.3    Van Nostrand, W.E.4
  • 32
    • 0030572751 scopus 로고    scopus 로고
    • Crosslinking of concanavalin A receptors on cortical neurons induces programmed cell death
    • Cribbs D. H., Kreng V. M., Anderson A. J., Cotman C. W. Crosslinking of concanavalin A receptors on cortical neurons induces programmed cell death. Neuroscience. 75:1996;173-185.
    • (1996) Neuroscience , vol.75 , pp. 173-185
    • Cribbs, D.H.1    Kreng, V.M.2    Anderson, A.J.3    Cotman, C.W.4
  • 33
    • 0028972701 scopus 로고
    • Image analysis of beta-amyloid load in Alzheimer's disease and relation to dementia severity
    • Cummings B. J., Cotman C. W. Image analysis of beta-amyloid load in Alzheimer's disease and relation to dementia severity. Lancet. 346:1995;1524-1528.
    • (1995) Lancet , vol.346 , pp. 1524-1528
    • Cummings, B.J.1    Cotman, C.W.2
  • 34
    • 0026718402 scopus 로고
    • Aggregation of the amyloid precursor protein within degenerating neurons and dystrophic neurites in Alzheimer's disease
    • Cummings B. J., Su J. H., Geddes J. W., van Nostrand W. E., Wagner S. L., Cunningham D. D., Cotman C. W. Aggregation of the amyloid precursor protein within degenerating neurons and dystrophic neurites in Alzheimer's disease. Neuroscience. 48(4):1992;763-777.
    • (1992) Neuroscience , vol.48 , Issue.4 , pp. 763-777
    • Cummings, B.J.1    Su, J.H.2    Geddes, J.W.3    Van Nostrand, W.E.4    Wagner, S.L.5    Cunningham, D.D.6    Cotman, C.W.7
  • 35
    • 0028807349 scopus 로고
    • Axon membrane flows from the growth cone to the cell body
    • Dai J., Sheetz M. P. Axon membrane flows from the growth cone to the cell body. Cell. 83:1995;693-701.
    • (1995) Cell , vol.83 , pp. 693-701
    • Dai, J.1    Sheetz, M.P.2
  • 38
    • 0025968644 scopus 로고
    • Inhibition of MAP2 expression affects both morphological and cell division phenotypes of neuronal differentation
    • Dinsmore J. H., Solomon F. Inhibition of MAP2 expression affects both morphological and cell division phenotypes of neuronal differentation. Cell. 64:1991;817-826.
    • (1991) Cell , vol.64 , pp. 817-826
    • Dinsmore, J.H.1    Solomon, F.2
  • 39
    • 0025166554 scopus 로고
    • Nucleotide and amino acid sequences of embryonic rat MAP2c
    • Doll, T., Papandrikopoulou, A. and Matus, A. (1990) Nucleotide and amino acid sequences of embryonic rat MAP2c. Nucleic Acids Res. 18-361.
    • (1990) Nucleic Acids Res. , pp. 18-361
    • Doll, T.1    Papandrikopoulou, A.2    Matus, A.3
  • 40
    • 0027519666 scopus 로고
    • An isoform of microtubule-associated protein 2 (MAP2) containing four repeats of the tubulin-binding motif
    • Doll T., Meichsner M., Riederer B. M., Honegger P., Matus A. An isoform of microtubule-associated protein 2 (MAP2) containing four repeats of the tubulin-binding motif. J. Cell Sci. 106:1993;633-640.
    • (1993) J. Cell Sci. , vol.106 , pp. 633-640
    • Doll, T.1    Meichsner, M.2    Riederer, B.M.3    Honegger, P.4    Matus, A.5
  • 41
    • 0030969575 scopus 로고    scopus 로고
    • MARK, a novel family of protein kinases that phosphorylate microtubule-associated proteins and trigger microtubule disruption
    • Drewes G., Ebneth A., Preuss U., Mandelkow E.-M., Mandelkow E. MARK, a novel family of protein kinases that phosphorylate microtubule-associated proteins and trigger microtubule disruption. Cell. 89:1997;297-308.
    • (1997) Cell , vol.89 , pp. 297-308
    • Drewes, G.1    Ebneth, A.2    Preuss, U.3    Mandelkow, E.-M.4    Mandelkow, E.5
  • 42
    • 0028026746 scopus 로고
    • Molecular motors are differentially distributed on Golgi membranes from polarized epithelial cells
    • Fath K. R., Trimbur G. M., Burgess D. R. Molecular motors are differentially distributed on Golgi membranes from polarized epithelial cells. J. Cell Biol. 126:1994;661-675.
    • (1994) J. Cell Biol. , vol.126 , pp. 661-675
    • Fath, K.R.1    Trimbur, G.M.2    Burgess, D.R.3
  • 43
    • 0028134711 scopus 로고
    • Sequence analysis of MAP2 function in living cells
    • Ferralli J., Doll T., Matus A. Sequence analysis of MAP2 function in living cells. J. Cell Sci. 107:1994;3115-3125.
    • (1994) J. Cell Sci. , vol.107 , pp. 3115-3125
    • Ferralli, J.1    Doll, T.2    Matus, A.3
  • 44
    • 0026606451 scopus 로고
    • Suppression of kinesin expression in cultured hippocampal neurons using antisense oligonucleotides
    • Ferreira A., Niclas J., Vale R. D., Banker G., Kosik K. Suppression of kinesin expression in cultured hippocampal neurons using antisense oligonucleotides. J. Cell Biol. 117:1992;5959-5966.
    • (1992) J. Cell Biol. , vol.117 , pp. 5959-5966
    • Ferreira, A.1    Niclas, J.2    Vale, R.D.3    Banker, G.4    Kosik, K.5
  • 45
    • 0029898806 scopus 로고    scopus 로고
    • Active transport of photoactivated tubulin molecules in growing axons revealed by a new electron microscopic analysis
    • Funakoshi T., Takeda S., Hirokawa N. Active transport of photoactivated tubulin molecules in growing axons revealed by a new electron microscopic analysis. J. Cell Biol. 133:1996;1347-1353.
    • (1996) J. Cell Biol. , vol.133 , pp. 1347-1353
    • Funakoshi, T.1    Takeda, S.2    Hirokawa, N.3
  • 46
    • 0026471340 scopus 로고
    • Effects of kinesin mutations on neuronal functions
    • Gho M., McDonald K., Ganetzky B., Saxton W. M. Effects of kinesin mutations on neuronal functions. Science. 258:1992;313-316.
    • (1992) Science , vol.258 , pp. 313-316
    • Gho, M.1    McDonald, K.2    Ganetzky, B.3    Saxton, W.M.4
  • 47
    • 0019781934 scopus 로고
    • Cilia and flagella of eukaryotes
    • Gibbons I. R. Cilia and flagella of eukaryotes. J. Cell Biol. 91:1981;107s-124s.
    • (1981) J. Cell Biol. , vol.91
    • Gibbons, I.R.1
  • 48
    • 0025600995 scopus 로고
    • Expression of separate isoforms of tau protein: Correlation with the tau pattern in brain and effects on tubulin polymerization
    • Goedert M., Jakes R. Expression of separate isoforms of tau protein: correlation with the tau pattern in brain and effects on tubulin polymerization. EMBO J. 9:1990;4225-4230.
    • (1990) EMBO J. , vol.9 , pp. 4225-4230
    • Goedert, M.1    Jakes, R.2
  • 49
    • 0027132479 scopus 로고
    • With apologies to Scheherazade: Tails of 1001 kinesin motors
    • Goldstein L. S. B. With apologies to Scheherazade: tails of 1001 kinesin motors. A. Rev. Genet. 27:1993;3199-3351.
    • (1993) A. Rev. Genet. , vol.27 , pp. 3199-3351
    • Goldstein, L.S.B.1
  • 50
    • 0019074235 scopus 로고
    • Intracellular transport in neurons
    • Grafstein B., Forman D. S. Intracellular transport in neurons. Physiol. Rev. 60:1980;1167-1283.
    • (1980) Physiol. Rev. , vol.60 , pp. 1167-1283
    • Grafstein, B.1    Forman, D.S.2
  • 51
    • 0026181461 scopus 로고
    • Stabilization and post-translational modification of microtubules during cellular morphogenesis
    • Gundersen G. G., Bulinski J. C. Stabilization and post-translational modification of microtubules during cellular morphogenesis. Bioessays. 13:1991;285-293.
    • (1991) Bioessays , vol.13 , pp. 285-293
    • Gundersen, G.G.1    Bulinski, J.C.2
  • 52
    • 0024453421 scopus 로고
    • Generation of a stable, posttranslationally modified microtubule array is an early event in myogenic differentiation
    • Gundersen G. G., Khawaja S., Bulinski J. C. Generation of a stable, posttranslationally modified microtubule array is an early event in myogenic differentiation. J. Cell Biol. 109:1989;2275-2288.
    • (1989) J. Cell Biol. , vol.109 , pp. 2275-2288
    • Gundersen, G.G.1    Khawaja, S.2    Bulinski, J.C.3
  • 53
    • 0002851512 scopus 로고
    • Axonal transport and the neuronal cytoskeleton
    • Eds. G. J. Siegel, B. W. Agranoff, R. W. Albers and P. B. Molinoff. Raven Press, New York
    • Hammerschlag, R. and Brady, S. T. (1989) Axonal Transport and the Neuronal Cytoskeleton. In Basic Neurochemistry, pp. 457-478. Eds. G. J. Siegel, B. W. Agranoff, R. W. Albers and P. B. Molinoff. Raven Press, New York.
    • (1989) In Basic Neurochemistry , pp. 457-478
    • Hammerschlag, R.1    Brady, S.T.2
  • 56
    • 0027358356 scopus 로고
    • Axonal transport and the cytoskeleton
    • Hirokawa N. Axonal transport and the cytoskeleton. Curr. Opin. Neurobiol. 3:1993;724-731.
    • (1993) Curr. Opin. Neurobiol. , vol.3 , pp. 724-731
    • Hirokawa, N.1
  • 57
    • 0024591237 scopus 로고
    • Submolecular domains of bovine brain kinesin identified by electron microscopy and monoclonal antibody decoration
    • Hirokawa N., Pfister K. K., Yorifuji H., Wagner M. C., Brady S. T., Bloom G. S. Submolecular domains of bovine brain kinesin identified by electron microscopy and monoclonal antibody decoration. Cell. 56:1989;867-878.
    • (1989) Cell , vol.56 , pp. 867-878
    • Hirokawa, N.1    Pfister, K.K.2    Yorifuji, H.3    Wagner, M.C.4    Brady, S.T.5    Bloom, G.S.6
  • 59
    • 0030479303 scopus 로고    scopus 로고
    • Centractin (ARP1) associates with spectrin revealing a potential mechanism to link dynactin to intracellular organelles
    • Holleran E. A., Tokito M. K., Karki S., Holzbaur E. L. F. Centractin (ARP1) associates with spectrin revealing a potential mechanism to link dynactin to intracellular organelles. J. Cell Biol. 135:1996;1815-1829.
    • (1996) J. Cell Biol. , vol.135 , pp. 1815-1829
    • Holleran, E.A.1    Tokito, M.K.2    Karki, S.3    Holzbaur, E.L.F.4
  • 60
    • 0028170819 scopus 로고
    • Dyneins: Molecular structure and cellular function
    • Holzbaur E. L., Vallee R. B. Dyneins: molecular structure and cellular function. A. Rev. Cell Biol. 10:1994;339-372.
    • (1994) A. Rev. Cell Biol. , vol.10 , pp. 339-372
    • Holzbaur, E.L.1    Vallee, R.B.2
  • 61
    • 0025135536 scopus 로고
    • Microtubule-associated protein 3 (MAP3) expression in non-neuronal tissues
    • Huber G., Matus A. Microtubule-associated protein 3 (MAP3) expression in non-neuronal tissues. J. Cell Sci. 95:1990;237-246.
    • (1990) J. Cell Sci. , vol.95 , pp. 237-246
    • Huber, G.1    Matus, A.2
  • 62
    • 0030068390 scopus 로고    scopus 로고
    • Mutation of the axonal transport motor kinesin enhances paralytic and suppresses Shaker in Drosophila
    • Hurd D. D., Stern M., Saxton W. M. Mutation of the axonal transport motor kinesin enhances paralytic and suppresses Shaker in Drosophila. Genetics. 142:1996;195-204.
    • (1996) Genetics , vol.142 , pp. 195-204
    • Hurd, D.D.1    Stern, M.2    Saxton, W.M.3
  • 63
    • 0024438227 scopus 로고
    • Expression of multiple isoforms and microtubule bundle formation in fibroblasts transfected with a single tau cDNA
    • Kanai Y., Takemura R., Oshima T., Mori H., Ihara Y., Yanangisawa M., Masaki T., Hirokawa N. Expression of multiple isoforms and microtubule bundle formation in fibroblasts transfected with a single tau cDNA. J. Cell Biol. 109:1989;1173-1184.
    • (1989) J. Cell Biol. , vol.109 , pp. 1173-1184
    • Kanai, Y.1    Takemura, R.2    Oshima, T.3    Mori, H.4    Ihara, Y.5    Yanangisawa, M.6    Masaki, T.7    Hirokawa, N.8
  • 64
    • 0028806377 scopus 로고
    • Affinity chromatography demonstrates a direct binding between cytoplasmic dynein and the dynactin complex
    • Karki S., Holzbaur E. L. Affinity chromatography demonstrates a direct binding between cytoplasmic dynein and the dynactin complex. J. biol. Chem. 270:1995;28806-28811.
    • (1995) J. Biol. Chem. , vol.270 , pp. 28806-28811
    • Karki, S.1    Holzbaur, E.L.2
  • 66
    • 0023877365 scopus 로고
    • Enhanced stability of microtubules enriched in detyrosinated tubulin is not a direct function of detyrosination level
    • Khawaja S., Gundersen G. G., Bulinski J. C. Enhanced stability of microtubules enriched in detyrosinated tubulin is not a direct function of detyrosination level. J. Cell Biol. 106:1988;141-149.
    • (1988) J. Cell Biol. , vol.106 , pp. 141-149
    • Khawaja, S.1    Gundersen, G.G.2    Bulinski, J.C.3
  • 67
    • 0029784022 scopus 로고    scopus 로고
    • Brain cytoplasmic and flagellar outer arm dyneins share a highly conserved Mr 8,000 light chain
    • King S. M., Barbarese E., Dillman J. F., Patel-King R. S., Carson J. H., Pfister K. K. Brain cytoplasmic and flagellar outer arm dyneins share a highly conserved Mr 8,000 light chain. J. biol. Chem. 271:1996;19358-19366.
    • (1996) J. Biol. Chem. , vol.271 , pp. 19358-19366
    • King, S.M.1    Barbarese, E.2    Dillman, J.F.3    Patel-King, R.S.4    Carson, J.H.5    Pfister, K.K.6
  • 72
    • 0028933382 scopus 로고
    • Kinectin, an essential anchor for kinesin-driven vesicle motility
    • Kumar J., Yu H., Sheetz M. P. Kinectin, an essential anchor for kinesin-driven vesicle motility. Science. 267:1995;1834-1837.
    • (1995) Science , vol.267 , pp. 1834-1837
    • Kumar, J.1    Yu, H.2    Sheetz, M.P.3
  • 74
    • 0026737638 scopus 로고
    • Microtubule-associated proteins 1A and LC2. Two proteins encoded in one messenger RNA
    • Langkopf A., Hammarback J. A., Muller R., Vallee R. B., Garner C. C. Microtubule-associated proteins 1A and LC2. Two proteins encoded in one messenger RNA. J. biol. Chem. 267:1992;16561-16566.
    • (1992) J. Biol. Chem. , vol.267 , pp. 16561-16566
    • Langkopf, A.1    Hammarback, J.A.2    Muller, R.3    Vallee, R.B.4    Garner, C.C.5
  • 75
    • 0022849722 scopus 로고
    • Polymer sliding in axons
    • Lasek R. J. Polymer sliding in axons. J. Cell Sci. 5s:1986;161-179.
    • (1986) J. Cell Sci. , vol.5 , pp. 161-179
    • Lasek, R.J.1
  • 77
    • 0026704256 scopus 로고
    • Expression of tau protein in non-neuronal cells: Microtubule binding and stabilization
    • Lee G., Rook S. L. Expression of tau protein in non-neuronal cells: microtubule binding and stabilization. J. Cell Sci. 102:1992;227-237.
    • (1992) J. Cell Sci. , vol.102 , pp. 227-237
    • Lee, G.1    Rook, S.L.2
  • 78
    • 0019815675 scopus 로고
    • Fodrin: Axonally transported polypeptides associated with the internal periphery of many cells
    • Levine J., Willard M. Fodrin: axonally transported polypeptides associated with the internal periphery of many cells. J. Cell Biol. 90:1981;631-643.
    • (1981) J. Cell Biol. , vol.90 , pp. 631-643
    • Levine, J.1    Willard, M.2
  • 79
    • 0024326799 scopus 로고
    • Organization of microtubules in dendrites and axons is determined by a short hydrophobic zipper in microtubule-associated proteins MAP2 and tau
    • Lewis, S. A., Ivanov, I. F., Lee, G. H. and Cowan, N. J. (1989) Organization of microtubules in dendrites and axons is determined by a short hydrophobic zipper in microtubule-associated proteins MAP2 and tau. Nature 342, 498-505 [Lewis, S. A. and Cowan, N. J. (correction) (1990) Nature 345, 674].
    • (1989) Nature , vol.342 , pp. 498-505
    • Lewis, S.A.1    Ivanov, I.F.2    Lee, G.H.3    Cowan, N.J.4
  • 80
    • 0025289620 scopus 로고
    • correction
    • Lewis, S. A., Ivanov, I. F., Lee, G. H. and Cowan, N. J. (1989) Organization of microtubules in dendrites and axons is determined by a short hydrophobic zipper in microtubule-associated proteins MAP2 and tau. Nature 342, 498-505 [Lewis, S. A. and Cowan, N. J. (correction) (1990) Nature 345, 674].
    • (1990) Nature , vol.345 , pp. 674
    • Lewis, S.A.1    Cowan, N.J.2
  • 81
    • 0029738637 scopus 로고    scopus 로고
    • Comparison of the intracellular distribution of cytoplasmic dynein and kinesin in cultured cells: Motor protein location does not reliably predict function
    • Lin S. X., Pfister K. K., Collins C. A. Comparison of the intracellular distribution of cytoplasmic dynein and kinesin in cultured cells: motor protein location does not reliably predict function. Cell Motil. Cytoskel. 34:1996;299-312.
    • (1996) Cell Motil. Cytoskel. , vol.34 , pp. 299-312
    • Lin, S.X.1    Pfister, K.K.2    Collins, C.A.3
  • 83
    • 0027533201 scopus 로고
    • Steric inhibition of cytoplasmic dynein and kinesin motility by MAP2
    • Lopez L., Sheetz M. P. Steric inhibition of cytoplasmic dynein and kinesin motility by MAP2. Cell Motil. Cytoskel. 24:1993;1-16.
    • (1993) Cell Motil. Cytoskel. , vol.24 , pp. 1-16
    • Lopez, L.1    Sheetz, M.P.2
  • 84
    • 0028999047 scopus 로고
    • A microtubule-associated protein (MAP2) kinase restores microtubule motility in embryonic brain
    • Lopez L., Sheetz M. P. A microtubule-associated protein (MAP2) kinase restores microtubule motility in embryonic brain. J. biol. Chem. 270:1995;12511-12517.
    • (1995) J. Biol. Chem. , vol.270 , pp. 12511-12517
    • Lopez, L.1    Sheetz, M.P.2
  • 85
    • 0023663075 scopus 로고
    • Identification of a microtubule-based cytoplasmic motor in the nematode C. elegans
    • Lye R. J., Porter M. E., Scholey J. M., McIntosh J. R. Identification of a microtubule-based cytoplasmic motor in the nematode C. elegans. Cell. 51:1987;309-318.
    • (1987) Cell , vol.51 , pp. 309-318
    • Lye, R.J.1    Porter, M.E.2    Scholey, J.M.3    McIntosh, J.R.4
  • 86
    • 0027367765 scopus 로고
    • β-amyloid precursor protein metabolites and loss of neuronal Ca++ homeostasis is Alzheimer's disease
    • Mattson M., Barger S., Cheng B., Lieberburg I., Smith-Swintosky V., Rydel R. β-amyloid precursor protein metabolites and loss of neuronal Ca++ homeostasis is Alzheimer's disease. TINS. 16:1993;409-414.
    • (1993) TINS , vol.16 , pp. 409-414
    • Mattson, M.1    Barger, S.2    Cheng, B.3    Lieberburg, I.4    Smith-Swintosky, V.5    Rydel, R.6
  • 87
    • 0028787443 scopus 로고
    • Regulation of cytoplasmic dynein function in vivo by the Drosophila Glued complex
    • McGrail M., Gepner J., Silvanovich A., Ludman S., Serr M., Hays T. S. Regulation of cytoplasmic dynein function in vivo by the Drosophila Glued complex. J. Cell Biol. 131:1995;411-425.
    • (1995) J. Cell Biol. , vol.131 , pp. 411-425
    • McGrail, M.1    Gepner, J.2    Silvanovich, A.3    Ludman, S.4    Serr, M.5    Hays, T.S.6
  • 88
    • 0022921987 scopus 로고
    • Diversity in the axonal transport of structural proteins: Major differences between optic and spinal axons in the rat
    • McQuarrie I. G., Brady S. T., Lasek R. J. Diversity in the axonal transport of structural proteins: major differences between optic and spinal axons in the rat. J. Neurosci. 6:1986;1593-1605.
    • (1986) J. Neurosci. , vol.6 , pp. 1593-1605
    • McQuarrie, I.G.1    Brady, S.T.2    Lasek, R.J.3
  • 89
    • 0030003894 scopus 로고    scopus 로고
    • Tubulin transport in neurons
    • Miller K. E., Joshi H. C. Tubulin transport in neurons. J. Cell Biol. 133:1996;1355-1366.
    • (1996) J. Cell Biol. , vol.133 , pp. 1355-1366
    • Miller, K.E.1    Joshi, H.C.2
  • 90
    • 0345432759 scopus 로고
    • Association of high molecular weight proteins with microtubules and their role in microtubule assembly in vitro
    • Murphy D. B., Borisy G. G. Association of high molecular weight proteins with microtubules and their role in microtubule assembly in vitro. Proc. natl. Acad. Sci. U.S.A. 72:1975;2696-2700.
    • (1975) Proc. Natl. Acad. Sci. U.S.A. , vol.72 , pp. 2696-2700
    • Murphy, D.B.1    Borisy, G.G.2
  • 91
    • 0028641560 scopus 로고
    • KIF1B, a novel microtubule plus end-directed monomeric motor protein for transport of mitochondria
    • Nangaku M., Sato-Yoshitake R., Okada Y., Noda Y., Takemura R., Yamazaki H., Hirokawa N. KIF1B, a novel microtubule plus end-directed monomeric motor protein for transport of mitochondria. Cell. 79:1994;1209-1220.
    • (1994) Cell , vol.79 , pp. 1209-1220
    • Nangaku, M.1    Sato-Yoshitake, R.2    Okada, Y.3    Noda, Y.4    Takemura, R.5    Yamazaki, H.6    Hirokawa, N.7
  • 92
    • 0031056220 scopus 로고    scopus 로고
    • Overexpression of full- or partial-length MAP4 stabilizes microtubules and alters cell growth
    • Nguyen L., Chari S., Lue C.-M., Gruber D., Chapin S., Bulinski J. C. Overexpression of full- or partial-length MAP4 stabilizes microtubules and alters cell growth. J. Cell Sci. 110:1997;281-294.
    • (1997) J. Cell Sci. , vol.110 , pp. 281-294
    • Nguyen, L.1    Chari, S.2    Lue, C.-M.3    Gruber, D.4    Chapin, S.5    Bulinski, J.C.6
  • 93
    • 0026781685 scopus 로고
    • A plus-end-directed motor enzyme that moves antiparallel microtubules in vitro localizes to the interzone of mitotic spindles
    • Nislow C., Lombillo V. A., Kuriyama R., McIntosh J. R. A plus-end-directed motor enzyme that moves antiparallel microtubules in vitro localizes to the interzone of mitotic spindles. Nature. 359:1992;543-547.
    • (1992) Nature , vol.359 , pp. 543-547
    • Nislow, C.1    Lombillo, V.A.2    Kuriyama, R.3    McIntosh, J.R.4
  • 94
    • 0028941998 scopus 로고
    • The activation of protein kinase A pathway selectively inhibits anterograde axonal transport of vesicles but not mitochondria transport or retrograde transport in vivo
    • Okada Y., Sato-Yoshitake R., Hirokawa N. The activation of protein kinase A pathway selectively inhibits anterograde axonal transport of vesicles but not mitochondria transport or retrograde transport in vivo. J. Neurosci. 15:1995;3053-3064.
    • (1995) J. Neurosci. , vol.15 , pp. 3053-3064
    • Okada, Y.1    Sato-Yoshitake, R.2    Hirokawa, N.3
  • 95
    • 0028927505 scopus 로고
    • Cyclin B interaction with microtubule-associated protein 4 (MAP4) targets p34cdc2 kinase to microtubules and is a potential regulator of M-phase microtubule dynamics
    • Ookata K., Hisanaga S., Bulinski J. C., Murofushi H., Aizawa H., Itoh T., Hotani H., Okumura E., Tachibana K., Kishimoto T. Cyclin B interaction with microtubule-associated protein 4 (MAP4) targets p34cdc2 kinase to microtubules and is a potential regulator of M-phase microtubule dynamics. J. Cell Biol. 128:1995;849-862.
    • (1995) J. Cell Biol. , vol.128 , pp. 849-862
    • Ookata, K.1    Hisanaga, S.2    Bulinski, J.C.3    Murofushi, H.4    Aizawa, H.5    Itoh, T.6    Hotani, H.7    Okumura, E.8    Tachibana, K.9    Kishimoto, T.10
  • 97
    • 0023608935 scopus 로고
    • MAP 1C is a microtubule-activated ATPase which translocates microtubules in vitro and has dynein-like properties
    • Paschal B. M., Shpetner H. S., Vallee R. B. MAP 1C is a microtubule-activated ATPase which translocates microtubules in vitro and has dynein-like properties. J. Cell Biol. 105:1987;1273-1282.
    • (1987) J. Cell Biol. , vol.105 , pp. 1273-1282
    • Paschal, B.M.1    Shpetner, H.S.2    Vallee, R.B.3
  • 98
    • 0345512210 scopus 로고
    • Anatomical Correlates of the distribution of the pathological changes in the Neocortex in Alzheimer's disease
    • Pearson R. C. A., Esiri M. M., Hioms R. W., Witlock G. K. P. Anatomical Correlates of the distribution of the pathological changes in the Neocortex in Alzheimer's disease. Proc. natl. Acad. Sci. U.S.A. 82:1985;4531-4534.
    • (1985) Proc. Natl. Acad. Sci. U.S.A. , vol.82 , pp. 4531-4534
    • Pearson, R.C.A.1    Esiri, M.M.2    Hioms, R.W.3    Witlock, G.K.P.4
  • 99
    • 0025992417 scopus 로고
    • In vitro aging of β-amyloid protein causes peptide aggregation and neurotoxicity
    • Pike C. J., Walencewicz A. J., Glabe C. G., Cotman C. W. In vitro aging of β-amyloid protein causes peptide aggregation and neurotoxicity. Brain Res. 563:1992;311-314.
    • (1992) Brain Res. , vol.563 , pp. 311-314
    • Pike, C.J.1    Walencewicz, A.J.2    Glabe, C.G.3    Cotman, C.W.4
  • 100
    • 0026671781 scopus 로고
    • β-amyloid induces neuritic dystrophy in vitro: Similarities with Alzheimer pathology
    • Pike C. J., Cummings B. J., Cotman C. W. β-amyloid induces neuritic dystrophy in vitro: similarities with Alzheimer pathology. Neuroreport. 3:1992;769-772.
    • (1992) Neuroreport , vol.3 , pp. 769-772
    • Pike, C.J.1    Cummings, B.J.2    Cotman, C.W.3
  • 101
    • 0025753031 scopus 로고
    • Microtubule polarity in Sertoli cells: A model for microtubule-based spermatid transport
    • Redenbach D. A., Vogl A. W. Microtubule polarity in Sertoli cells: a model for microtubule-based spermatid transport. Eur. J. Cell Biol. 54:1991;277-290.
    • (1991) Eur. J. Cell Biol. , vol.54 , pp. 277-290
    • Redenbach, D.A.1    Vogl, A.W.2
  • 102
    • 0000146080 scopus 로고
    • Differential expression of distinct microtubule-associated proteins during brain development
    • Riederer B., Matus A. Differential expression of distinct microtubule-associated proteins during brain development. Proc. natl. Acad. Sci. U.S.A. 82:1985;6006-6009.
    • (1985) Proc. Natl. Acad. Sci. U.S.A. , vol.82 , pp. 6006-6009
    • Riederer, B.1    Matus, A.2
  • 103
    • 0030939131 scopus 로고    scopus 로고
    • KIFC2 is a novel neuron-specific C-terminal type kinesin superfamily motor for dendritic transport of multivesicular body-like organelles
    • Saito N., Okada Y., Noda Y., Kinoshita Y., Kondo S., Hirokawa N. KIFC2 is a novel neuron-specific C-terminal type kinesin superfamily motor for dendritic transport of multivesicular body-like organelles. Neuron. 18:1997;425-438.
    • (1997) Neuron , vol.18 , pp. 425-438
    • Saito, N.1    Okada, Y.2    Noda, Y.3    Kinoshita, Y.4    Kondo, S.5    Hirokawa, N.6
  • 104
    • 0023473468 scopus 로고
    • Axonal and transbeuronal transport in the transmission of neurological disease: Potential role in systems degeneration including Alzheimer's disease
    • Saper C. B., Wainer B. H., German D. C. Axonal and transbeuronal transport in the transmission of neurological disease: potential role in systems degeneration including Alzheimer's disease. Neuroscience. 23:1987;389-398.
    • (1987) Neuroscience , vol.23 , pp. 389-398
    • Saper, C.B.1    Wainer, B.H.2    German, D.C.3
  • 106
    • 0028304474 scopus 로고
    • Ultrastructural analysis of the dynactin complex: An actin-related protein is a component of a filament that resembles F-actin
    • Schafer D. A., Gill S. R., Cooper J. A., Heuser J. E., Schroer T. A. Ultrastructural analysis of the dynactin complex: an actin-related protein is a component of a filament that resembles F-actin. J. Cell Biol. 126:1994;403-412.
    • (1994) J. Cell Biol. , vol.126 , pp. 403-412
    • Schafer, D.A.1    Gill, S.R.2    Cooper, J.A.3    Heuser, J.E.4    Schroer, T.A.5
  • 107
    • 0028146484 scopus 로고
    • New insights into the interaction of cytoplasmic dynein with the actin-related protein, Arp1
    • Schroer T. A. New insights into the interaction of cytoplasmic dynein with the actin-related protein, Arp1. J. Cell Biol. 127:1994;1-4.
    • (1994) J. Cell Biol. , vol.127 , pp. 1-4
    • Schroer, T.A.1
  • 108
    • 0024604298 scopus 로고
    • Cytoplasmic dynein is a minus end-directed motor for membranous organelles
    • Schroer T. A., Steuer E. R., Sheetz M. P. Cytoplasmic dynein is a minus end-directed motor for membranous organelles. Cell. 56:1989;937-946.
    • (1989) Cell , vol.56 , pp. 937-946
    • Schroer, T.A.1    Steuer, E.R.2    Sheetz, M.P.3
  • 109
    • 0023292950 scopus 로고
    • Dynamic and stable populations of microtubules in cells
    • Schulze E., Kirschner M. Dynamic and stable populations of microtubules in cells. J. Cell Biol. 104:1987;277-288.
    • (1987) J. Cell Biol. , vol.104 , pp. 277-288
    • Schulze, E.1    Kirschner, M.2
  • 110
    • 0029069185 scopus 로고
    • Transport of dendritic microtubules establishes their nonuniform polarity orientation
    • Sharp D. J., Yu W., Baas P. W. Transport of dendritic microtubules establishes their nonuniform polarity orientation. J. Cell Biol. 130:1995;93-103.
    • (1995) J. Cell Biol. , vol.130 , pp. 93-103
    • Sharp, D.J.1    Yu, W.2    Baas, P.W.3
  • 111
    • 0029947691 scopus 로고    scopus 로고
    • Expression of kinesin-related motor protein induces Sf9 cells to form dendrite-like processes with nonuniform microtubule polarity orientation
    • Sharp D. J., Kuriyama R., Baas P. W. Expression of kinesin-related motor protein induces Sf9 cells to form dendrite-like processes with nonuniform microtubule polarity orientation. J. Neurosci. 16:1996;4375.
    • (1996) J. Neurosci. , vol.16 , pp. 4375
    • Sharp, D.J.1    Kuriyama, R.2    Baas, P.W.3
  • 112
    • 0001065402 scopus 로고    scopus 로고
    • Regulation of kinesin and cytoplasmic dynein-driven organelle motility
    • Sheetz M. P., Yu H. Regulation of kinesin and cytoplasmic dynein-driven organelle motility. Semin. Cell Dev. Biol. 7:1996;329-334.
    • (1996) Semin. Cell Dev. Biol. , vol.7 , pp. 329-334
    • Sheetz, M.P.1    Yu, H.2
  • 114
    • 0030295320 scopus 로고    scopus 로고
    • Immunogold localization of the intermediate chain within the protein complex of cytoplasmic dynein
    • Steffen W., Hodgkinson J. L., Wiche G. Immunogold localization of the intermediate chain within the protein complex of cytoplasmic dynein. J. Struct. Biol. 117:1996;227-235.
    • (1996) J. Struct. Biol. , vol.117 , pp. 227-235
    • Steffen, W.1    Hodgkinson, J.L.2    Wiche, G.3
  • 115
    • 0030574061 scopus 로고    scopus 로고
    • Alzheimer's disease amyloid precursor protein on the surface of corticaö neurons in primary culture co-localizes with adhesion patch components
    • Storey E., Beyreuther K., Masters C. L. Alzheimer's disease amyloid precursor protein on the surface of corticaö neurons in primary culture co-localizes with adhesion patch components. Brain Res. 735:1996;217-231.
    • (1996) Brain Res. , vol.735 , pp. 217-231
    • Storey, E.1    Beyreuther, K.2    Masters, C.L.3
  • 116
    • 0028835801 scopus 로고
    • Apoptosis. Death of a T cell [news; Comment]
    • Strasser A. Apoptosis. Death of a T cell [news; comment]. Nature. 373:1995;385-386.
    • (1995) Nature , vol.373 , pp. 385-386
    • Strasser, A.1
  • 119
    • 0029742626 scopus 로고    scopus 로고
    • Functionally distinct isoforms of dynactin are expressed in human neurons
    • Tokito M. K., Howland D. S., Lee V. M., Holzbaur E. L. Functionally distinct isoforms of dynactin are expressed in human neurons. Molec. biol. Cell. 7:1996;1167-1180.
    • (1996) Molec. Biol. Cell , vol.7 , pp. 1167-1180
    • Tokito, M.K.1    Howland, D.S.2    Lee, V.M.3    Holzbaur, E.L.4
  • 120
    • 0030604661 scopus 로고    scopus 로고
    • Kinectin distribution in chicken nervous system
    • Toyoshima I., Sheetz M. P. Kinectin distribution in chicken nervous system. Neurosci. Lett. 211:1996;1-4.
    • (1996) Neurosci. Lett. , vol.211 , pp. 1-4
    • Toyoshima, I.1    Sheetz, M.P.2
  • 121
  • 122
    • 0022385727 scopus 로고
    • Identification of a novel force-generating protein, kinesin, involved in microtubule-based motility
    • Vale R. D., Reese T. S., Sheetz M. P. Identification of a novel force-generating protein, kinesin, involved in microtubule-based motility. Cell. 42:1985;39-50.
    • (1985) Cell , vol.42 , pp. 39-50
    • Vale, R.D.1    Reese, T.S.2    Sheetz, M.P.3
  • 123
    • 0022294771 scopus 로고
    • Different axoplasmic proteins generate movement in opposite directions along microtubules in vitro
    • Vale R. D., Schnapp B. J., Mitchison T., Steuer E., Reese T. S., Sheetz M. P. Different axoplasmic proteins generate movement in opposite directions along microtubules in vitro. Cell. 43:1985;623-632.
    • (1985) Cell , vol.43 , pp. 623-632
    • Vale, R.D.1    Schnapp, B.J.2    Mitchison, T.3    Steuer, E.4    Reese, T.S.5    Sheetz, M.P.6
  • 124
    • 0029932027 scopus 로고    scopus 로고
    • Targeting of motor proteins
    • Vallee R. B., Sheetz M. P. Targeting of motor proteins. Science. 271:1996;1539-1544.
    • (1996) Science , vol.271 , pp. 1539-1544
    • Vallee, R.B.1    Sheetz, M.P.2
  • 125
    • 0025894107 scopus 로고
    • Proteins of the mammalian mitotic spindle: Phosphorylation/dephosphorylation of MAP4 during mitosis
    • Vandré D. D., Centonze V. E., Peloquin J., Tombes R. M., Borisy G. G. Proteins of the mammalian mitotic spindle: phosphorylation/dephosphorylation of MAP4 during mitosis. J. Cell Sci. 98:1991;577-588.
    • (1991) J. Cell Sci. , vol.98 , pp. 577-588
    • Vandré, D.D.1    Centonze, V.E.2    Peloquin, J.3    Tombes, R.M.4    Borisy, G.G.5
  • 126
    • 0029563632 scopus 로고
    • Cytoplasmic dynein binds dynactin through a direct interaction between the intermediate chains and p150glued
    • Vaughan K. T., Vallee R. B. Cytoplasmic dynein binds dynactin through a direct interaction between the intermediate chains and p150glued. J. Cell Biol. 131:1995;1507-1516.
    • (1995) J. Cell Biol. , vol.131 , pp. 1507-1516
    • Vaughan, K.T.1    Vallee, R.B.2
  • 127
    • 0011214518 scopus 로고    scopus 로고
    • Removal of MAP4 from microtubules in vivo produces no discernible phenotype at the cellular level
    • Wang X. M., Peloquin J. J., Zhai Y., Bulinski J. C., Borisy G. G. Removal of MAP4 from microtubules in vivo produces no discernible phenotype at the cellular level. J. Cell Biol. 132:1996;349-358.
    • (1996) J. Cell Biol. , vol.132 , pp. 349-358
    • Wang, X.M.1    Peloquin, J.J.2    Zhai, Y.3    Bulinski, J.C.4    Borisy, G.G.5
  • 128
    • 0028859428 scopus 로고
    • Single cytoplasmic dynein molecule movements: Characterization and comparison with kinesin
    • Wang Z., Khan S., Sheetz M. P. Single cytoplasmic dynein molecule movements: characterization and comparison with kinesin. Biophys. J. 69:1995;2011-2023.
    • (1995) Biophys. J. , vol.69 , pp. 2011-2023
    • Wang, Z.1    Khan, S.2    Sheetz, M.P.3
  • 129
    • 0028986631 scopus 로고
    • The p150Glued component of the dynactin complex binds to both microtubules and the actin-related protein centractin (Arp-1)
    • Waterman-Storer C. M., Karki S., Holzbaur E. L. The p150Glued component of the dynactin complex binds to both microtubules and the actin-related protein centractin (Arp-1). Proc. natl. Acad. Sci. U.S.A. 92:1995;1634-1638.
    • (1995) Proc. Natl. Acad. Sci. U.S.A. , vol.92 , pp. 1634-1638
    • Waterman-Storer, C.M.1    Karki, S.2    Holzbaur, E.L.3
  • 130
    • 0023406178 scopus 로고
    • Turnover of the carboxy-terminal tyrosine of alpha-tubulin and means of reaching elevated levels of detyrosination in living cells
    • Wehland J., Weber K. Turnover of the carboxy-terminal tyrosine of alpha-tubulin and means of reaching elevated levels of detyrosination in living cells. J. Cell Sci. 88:1987;185-193.
    • (1987) J. Cell Sci. , vol.88 , pp. 185-193
    • Wehland, J.1    Weber, K.2
  • 131
    • 0025837142 scopus 로고
    • A model for microtubule-associated protein 4 structure
    • West R. R., Tenbarge K. M., Olmsted J. B. A model for microtubule-associated protein 4 structure. J. biol. Chem. 266:1991;21886-21896.
    • (1991) J. Biol. Chem. , vol.266 , pp. 21886-21896
    • West, R.R.1    Tenbarge, K.M.2    Olmsted, J.B.3
  • 132
    • 0025095256 scopus 로고
    • β-amyloid protein promotes neuritic branching in hippocampal cultures
    • Whitson J. S., Glabe C. G., Shitani E., Abcar A., Cotman C. W. β-amyloid protein promotes neuritic branching in hippocampal cultures. Neurosci. Lett. 110:1990;319-324.
    • (1990) Neurosci. Lett. , vol.110 , pp. 319-324
    • Whitson, J.S.1    Glabe, C.G.2    Shitani, E.3    Abcar, A.4    Cotman, C.W.5
  • 134
    • 0028913471 scopus 로고
    • Trafficking of cell surface β-amyloid precursor protein: Retrograge and transcyotic transport in cultured neurons
    • Yamazaki T., Selkoe D. J., Koo E. H. Trafficking of cell surface β-amyloid precursor protein: retrograge and transcyotic transport in cultured neurons. J. Cell Biol. 129:1995;431-442.
    • (1995) J. Cell Biol. , vol.129 , pp. 431-442
    • Yamazaki, T.1    Selkoe, D.J.2    Koo, E.H.3
  • 135
    • 0026758070 scopus 로고
    • Kinesin and cytoplasmic dynein binding to brain microsomes
    • Yu H., Toyoshima I., Steuer E. R., Sheetz M. P. Kinesin and cytoplasmic dynein binding to brain microsomes. J. biol. Chem. 267:1992;20457-20464.
    • (1992) J. Biol. Chem. , vol.267 , pp. 20457-20464
    • Yu, H.1    Toyoshima, I.2    Steuer, E.R.3    Sheetz, M.P.4
  • 136
    • 0029979555 scopus 로고    scopus 로고
    • Microtubule transport and assembly during growth
    • Yu W., Schwei M. J., Baas P. W. Microtubule transport and assembly during growth. J. Cell Biol. 133:1996;151-157.
    • (1996) J. Cell Biol. , vol.133 , pp. 151-157
    • Yu, W.1    Schwei, M.J.2    Baas, P.W.3
  • 137
    • 0031050564 scopus 로고    scopus 로고
    • Inhibition of a mitotic motor compromises the formation of dendrite-like processes from neuroblastoma cells
    • Yu W., Sharp D. J., Kuriyama R., Mallik P., Baas P. W. Inhibition of a mitotic motor compromises the formation of dendrite-like processes from neuroblastoma cells. J. Cell Biol. 136:1997;659-668.
    • (1997) J. Cell Biol. , vol.136 , pp. 659-668
    • Yu, W.1    Sharp, D.J.2    Kuriyama, R.3    Mallik, P.4    Baas, P.W.5
  • 138
    • 0028231706 scopus 로고
    • Quantitative determination of the proportion of microtubule polymer present during the mitosis-interphase transition
    • Zhai Y., Borisy G. G. Quantitative determination of the proportion of microtubule polymer present during the mitosis-interphase transition. J. Cell Sci. 107:1994;881-890.
    • (1994) J. Cell Sci. , vol.107 , pp. 881-890
    • Zhai, Y.1    Borisy, G.G.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.